Affinity-Based Selectivity Profiling of an In-Class Selective Competitive Inhibitor of Acyl Protein Thioesterase 2
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https://figshare.com/articles/dataset/Affinity-Based_Selectivity_Profiling_of_an_In-Class_Selective_Competitive_Inhibitor_of_Acyl_Protein_Thioesterase_2/4483739
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资源简介：
Activity-based
protein profiling (ABPP) has revolutionized the
discovery and optimization of active-site ligands across distinct
enzyme families, providing a robust platform for in-class selectivity
profiling. Nonetheless, this approach is less straightforward for
profiling reversible inhibitors and does not access proteins outside
the ABPP probe’s target profile. While the active-site competitive
acyl protein thioesterase 2 inhibitor ML349 (Ki = 120 nM) is highly selective within the serine hydrolase
enzyme family, it could still interact with other cellular targets.
Here we present a chemoproteomic workflow to enrich and profile candidate
ML349-binding proteins. In human cell lysates, biotinylated-ML349
enriches a recurring set of proteins, including metabolite kinases
and flavin-dependent oxidoreductases that are potentially enhanced
by avidity-driven multimeric interactions. Confirmatory assays by
native mass spectrometry and fluorescence polarization quickly rank-ordered
these weak off-targets, providing justification to explore ligand
interactions and stoichiometry beyond ABPP.
创建时间：
2016-12-20
